|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00150 |
PTZ00150 |
phosphoglucomutase-2-like protein; Provisional |
24-642 |
0e+00 |
|
phosphoglucomutase-2-like protein; Provisional
Pssm-ID: 240294 Cd Length: 584 Bit Score: 750.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 24 QLDTAIGQWLRWDKlqgrlawcpgrrvehdscflqNPKTKEQIENLLRNGMNKELRDRLCCRMTFGTAGLRSAMGAGFCY 103
Cdd:PTZ00150 4 SLEAQVELWLKWDK---------------------DPETRKEIEELLASKDEEELKRRFLKRMEFGTAGLRGKMGAGFNC 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 104 INDLTVIQSTQGMYKYLERCFS-DFKQRGFVVGYDTRGQvtsscsSQRLAKLTAAVLLAKDVPVYLFSRYVPTPFVPYAV 182
Cdd:PTZ00150 63 MNDLTVQQTAQGLCAYVIETFGqALKSRGVVIGYDGRYH------SRRFAEITASVFLSKGFKVYLFGQTVPTPFVPYAV 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 183 QKLKAVAGVMITASHNRKEDNGYKVYWETGAQITSPHDKEILKCIEECVEPWNGSWNDNlvdTSPLKRDPLQDICRRYME 262
Cdd:PTZ00150 137 RKLKCLAGVMVTASHNPKEDNGYKVYWSNGAQIIPPHDKNISAKILSNLEPWSSSWEYL---TETLVEDPLAEVSDAYFA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 263 DLKKI-CFYRELNSKttLKFVHTSFHGVGHDYVQLAFKVFGFKPPIPVPEQKDPDPDFSTVKCPNPEEGESVLELSLRLA 341
Cdd:PTZ00150 214 TLKSEyNPACCDRSK--VKIVYTAMHGVGTRFVQKALHTVGLPNLLSVAQQAEPDPEFPTVTFPNPEEGKGALKLSMETA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 342 EKENARVVLATDPDADRLAAAELQENGcWKVFTGNELAALFGWWMfdcWKKNKSRNADVKNVYMLATTVSSKILKAIALK 421
Cdd:PTZ00150 292 EAHGSTVVLANDPDADRLAVAEKLNNG-WKIFTGNELGALLAWWA---MKRYRRQGIDKSKCFFICTVVSSRMLKKMAEK 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 422 EGFHFEETLPGFKWIGSRIIDLL-ENGKEVLFAFEESIGFLCGTSVLDKDGVSAAVVVAEMASYLETMNITLKQQLVKVY 500
Cdd:PTZ00150 368 EGFQYDETLTGFKWIGNKAIELNaENGLTTLFAYEEAIGFMLGTRVRDKDGVTAAAVVAEMALYLYERGKTLVEHLESLY 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 501 EKYGYHISKTSYFLCYEPPTIKSIFERLRNFDSpkeYPKFCGTFAILHVRDVTTGYDSSQPNKKSVLPVSKNSQMITFTF 580
Cdd:PTZ00150 448 KQYGYHFTNNSYYICYDPSRIVSIFNDIRNNGS---YPTKLGGYPVTRIRDLTTGYDTATPDGKPLLPVSASTQMITFYF 524
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767967976 581 QNGCVATLRTSGTEPKIKYYAEMCASPDQSdtalLEEELKKLIDALIENFLQPSKNGLIWRS 642
Cdd:PTZ00150 525 ENGAIITIRGSGTEPKLKWYAELSGTKDEA----VEKELAALVDEVVEQLMQPEKYGLVPRK 582
|
|
| PGM2 |
cd05799 |
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The ... |
85-628 |
0e+00 |
|
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The mammalian PGM2 is thought to be a phosphopentomutase that catalyzes the conversion of the nucleoside breakdown products, ribose-1-phosphate and deoxyribose-1-phosphate to the corresponding 5-phosphopentoses. PGM2L1 is thought to catalyze the 1,3-bisphosphoglycerate-dependent synthesis of glucose 1,6-bisphosphate and other aldose-bisphosphates that serve as cofactors for several sugar phosphomutases and possibly also as regulators of glycolytic enzymes. PGM2 and PGM2L1 belong to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100092 Cd Length: 487 Bit Score: 680.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 85 RMTFGTAGLRSAMGAGFCYINDLTVIQSTQGMYKYLERCFSDFKQRGFVVGYDTRGqvtsscSSQRLAKLTAAVLLAKDV 164
Cdd:cd05799 1 RLEFGTAGLRGKMGAGTNRMNDYTVRQATQGLANYLKKKGPDAKNRGVVIGYDSRH------NSREFAELTAAVLAANGI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 165 PVYLFSRYVPTPFVPYAVQKLKAVAGVMITASHNRKEDNGYKVYWETGAQITSPHDKEILKCIEECVEPWNGSWNDNLvd 244
Cdd:cd05799 75 KVYLFDDLRPTPLLSFAVRHLGADAGIMITASHNPKEYNGYKVYWEDGAQIIPPHDAEIAEEIEAVLEPLDIKFEEAL-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 245 TSPLKRDPLQDICRRYMEDLKKICFYRELNSKTTLKFVHTSFHGVGHDYVQLAFKVFGFKPPIPVPEQKDPDPDFSTVKC 324
Cdd:cd05799 153 DSGLIKYIGEEIDDAYLEAVKKLLVNPELNEGKDLKIVYTPLHGVGGKFVPRALKEAGFTNVIVVEEQAEPDPDFPTVKF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 325 PNPEEgESVLELSLRLAEKENARVVLATDPDADRLAAAELQENGCWKVFTGNELAALFGWWMFDCWKKNKSrnaDVKNVY 404
Cdd:cd05799 233 PNPEE-PGALDLAIELAKKVGADLILATDPDADRLGVAVKDKDGEWRLLTGNEIGALLADYLLEQRKEKGK---LPKNPV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 405 MLATTVSSKILKAIALKEGFHFEETLPGFKWIGSRIIDLLENGKEVLFAFEESIGFLCGTSVLDKDGVSAAVVVAEMASY 484
Cdd:cd05799 309 IVKTIVSSELLRKIAKKYGVKVEETLTGFKWIGNKIEELESGGKKFLFGFEESIGYLVGPFVRDKDGISAAALLAEMAAY 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 485 LETMNITLKQQLVKVYEKYGYHISKTSYFLCYE---PPTIKSIFERLRNfdspkeypkfcgtfailhvrdvttgydssqp 561
Cdd:cd05799 389 LKAQGKTLLDRLDELYEKYGYYKEKTISITFEGkegPEKIKAIMDRLRN------------------------------- 437
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767967976 562 nkksvlpvskNSQMITFTFQNGCVATLRTSGTEPKIKYYAEMCASPDqsdtallEEELKKLIDALIE 628
Cdd:cd05799 438 ----------NPNVLTFYLEDGSRVTVRPSGTEPKIKFYIEVVGKKT-------LEEAEKKLDALKK 487
|
|
| ManB |
COG1109 |
Phosphomannomutase [Carbohydrate transport and metabolism]; |
85-627 |
1.26e-85 |
|
Phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440726 [Multi-domain] Cd Length: 456 Bit Score: 275.54 E-value: 1.26e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 85 RMTFGTAGLRSAMGAgfcYINDLTVIQSTQGMYKYLERCfsdfKQRGFVVGYDTRgqvtssCSSQRLAKLTAAVLLAKDV 164
Cdd:COG1109 4 KKLFGTDGIRGIVGE---ELTPEFVLKLGRAFGTYLKEK----GGPKVVVGRDTR------LSSPMLARALAAGLASAGI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 165 PVYLFsRYVPTPFVPYAVQKLKAVAGVMITASHNRKEDNGYKVYWETGAQITSPHDKEILKCIEEcVEPWNGSWNDNlvd 244
Cdd:COG1109 71 DVYDL-GLVPTPALAFAVRHLGADGGIMITASHNPPEYNGIKFFDADGGKLSPEEEKEIEALIEK-EDFRRAEAEEI--- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 245 tSPLKRdpLQDICRRYMEDLKKicFYRELNSKTTLKFVHTSFHGVGHDYVQLAFKVFGFKpPIPVPEQkdPDPDFSTVKc 324
Cdd:COG1109 146 -GKVTR--IEDVLEAYIEALKS--LVDEALRLRGLKVVVDCGNGAAGGVAPRLLRELGAE-VIVLNAE--PDGNFPNHN- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 325 PNPEEGesVLELSLRLAEKENARVVLATDPDADRLAAAElqENGcwKVFTGNELAALFGWWMfdcwkKNKSRNADVknvy 404
Cdd:COG1109 217 PNPEPE--NLEDLIEAVKETGADLGIAFDGDADRLGVVD--EKG--RFLDGDQLLALLARYL-----LEKGPGGTV---- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 405 mLATTVSSKILKAIALKEGFHFEETLPGFKWIGSRIidlLENGkeVLFAFEESIGFLCGTSVLDKDGVSAAVVVAEMASY 484
Cdd:COG1109 282 -VVTVMSSLALEDIAEKHGGEVVRTKVGFKYIKEKM---RETG--AVLGGEESGGIIFPDFVPTDDGILAALLLLELLAK 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 485 LETmniTLKQqlvkVYEKYGYHISKTSYFLCYEPPTIKSIFERLRNfdspkeypkfcgtfAILHVRDVTTgydssqpnkk 564
Cdd:COG1109 356 QGK---SLSE----LLAELPRYPQPEINVRVPDEEKIGAVMEKLRE--------------AVEDKEELDT---------- 404
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767967976 565 svlpvsknSQMITFTFQNGCVATLRTSGTEPKIKYYAEmcaSPDQSDTALLEEELKKLIDALI 627
Cdd:COG1109 405 --------IDGVKVDLEDGGWVLVRPSGTEPLLRVYAE---AKDEEEAEELLAELAELVEEAL 456
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
85-229 |
1.54e-38 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
Pssm-ID: 427032 Cd Length: 138 Bit Score: 138.90 E-value: 1.54e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 85 RMTFGTAGLRSAMGAGFcyINDLTVIQSTQGMYKYLErcfSDFKQRGFVVGYDTRGqvtsscSSQRLAKLTAAVLLAKDV 164
Cdd:pfam02878 1 RQLFGTSGIRGKVGVGE--LTPEFALKLGQAIASYLR---AQGGGGKVVVGRDTRY------SSRELARALAAGLASNGV 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767967976 165 PVYLFSrYVPTPFVPYAVQKLKAVAGVMITASHNRKEDNGYKVYWETGAQITSPHDKEILKCIEE 229
Cdd:pfam02878 70 EVILLG-LLPTPAVSFATRKLKADGGIMITASHNPPEYNGIKVFDSNGGPIPPEVEKKIEAIIEK 133
|
|
| Arch_GlmM |
TIGR03990 |
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ... |
133-623 |
4.99e-27 |
|
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been characterized as the archaeal protein responsible for the second step of UDP-GlcNAc biosynthesis. This GlmM protein catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate. The first-characterized bacterial GlmM protein is modeled by TIGR01455. These two families are members of the larger phosphoglucomutase/phosphomannomutase family (characterized by three domains: pfam02878, pfam02879 and pfam02880), but are not nearest neighbors to each other. This model also includes a number of sequences from non-archaea in the Bacteroides, Chlorobi, Chloroflexi, Planctomycetes and Spirochaetes lineages. Evidence supporting their inclusion in this equivalog as having the same activity comes from genomic context and phylogenetic profiling. A large number of these organisms are known to produce exo-polysaccharide and yet only appeared to contain the GlmS enzyme of the GlmSMU pathway for UDP-GlcNAc biosynthesis (GenProp0750). In some organisms including Leptospira, this archaeal GlmM is found adjacent to the GlmS as well as a putative GlmU non-orthologous homolog. Phylogenetic profiling of the GlmS-only pattern using PPP identifies members of this archaeal GlmM family as the highest-scoring result. [Central intermediary metabolism, Amino sugars]
Pssm-ID: 274906 Cd Length: 443 Bit Score: 114.53 E-value: 4.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 133 VVGYDTRgqvtssCSSQRLAKLTAAVLLAKDVPVYLFSrYVPTPFVPYAVQKLKAVAGVMITASHNRKEDNGYKVYWETG 212
Cdd:TIGR03990 39 VVGRDTR------TSGPMLENAVIAGLLSTGCDVVDLG-IAPTPTLQYAVRELGADGGIMITASHNPPEYNGIKLLNSDG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 213 AQITSPHDKEILKCIEE---CVEPWNGswndnlvdTSPLKRDPlqDICRRYMED-LKKICfyRELNSKTTLKFVHTSFHG 288
Cdd:TIGR03990 112 TELSREQEEEIEEIAESgdfERADWDE--------IGTVTSDE--DAIDDYIEAiLDKVD--VEAIRKKGFKVVVDCGNG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 289 VGHDYVQLAFKVFGFKpPIPVPEQkdPDPDFSTvkcPNPEEGESVLELSLRLAEKENARVVLATDPDADRLAAaeLQENG 368
Cdd:TIGR03990 180 AGSLTTPYLLRELGCK-VITLNCQ--PDGTFPG---RNPEPTPENLKDLSALVKATGADLGIAHDGDADRLVF--IDEKG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 369 cwKVFTGNELAALFGWWMfdcWKKNKSRnadvknvymLATTVS-SKILKAIALKEGFHFEETLpgfkwIGSRII--DLLE 445
Cdd:TIGR03990 252 --RFIGGDYTLALFAKYL---LEHGGGK---------VVTNVSsSRAVEDVAERHGGEVIRTK-----VGEVNVaeKMKE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 446 NGkeVLFAFEESIGFLCGTSVLDKDGVSAAVVVAEMasyLETMNITLkQQLVKVYEKygYHISKTSyflcYEPPTIK--S 523
Cdd:TIGR03990 313 EG--AVFGGEGNGGWIFPDHHYCRDGLMAAALFLEL---LAEEGKPL-SELLAELPK--YPMSKEK----VELPDEDkeE 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 524 IFERLRnfdspKEYPKFcgtfailhvrDVTT--GydssqpnkksvlpvsknsqmITFTFQNGCVaTLRTSGTEPKIKYYA 601
Cdd:TIGR03990 381 VMEAVE-----EEFADA----------EIDTidG--------------------VRIDFEDGWV-LVRPSGTEPIVRIYA 424
|
490 500
....*....|....*....|..
gi 767967976 602 EmcaSPDQSDTALLEEELKKLI 623
Cdd:TIGR03990 425 E---AKTEERAEELLEEGRSLV 443
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00150 |
PTZ00150 |
phosphoglucomutase-2-like protein; Provisional |
24-642 |
0e+00 |
|
phosphoglucomutase-2-like protein; Provisional
Pssm-ID: 240294 Cd Length: 584 Bit Score: 750.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 24 QLDTAIGQWLRWDKlqgrlawcpgrrvehdscflqNPKTKEQIENLLRNGMNKELRDRLCCRMTFGTAGLRSAMGAGFCY 103
Cdd:PTZ00150 4 SLEAQVELWLKWDK---------------------DPETRKEIEELLASKDEEELKRRFLKRMEFGTAGLRGKMGAGFNC 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 104 INDLTVIQSTQGMYKYLERCFS-DFKQRGFVVGYDTRGQvtsscsSQRLAKLTAAVLLAKDVPVYLFSRYVPTPFVPYAV 182
Cdd:PTZ00150 63 MNDLTVQQTAQGLCAYVIETFGqALKSRGVVIGYDGRYH------SRRFAEITASVFLSKGFKVYLFGQTVPTPFVPYAV 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 183 QKLKAVAGVMITASHNRKEDNGYKVYWETGAQITSPHDKEILKCIEECVEPWNGSWNDNlvdTSPLKRDPLQDICRRYME 262
Cdd:PTZ00150 137 RKLKCLAGVMVTASHNPKEDNGYKVYWSNGAQIIPPHDKNISAKILSNLEPWSSSWEYL---TETLVEDPLAEVSDAYFA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 263 DLKKI-CFYRELNSKttLKFVHTSFHGVGHDYVQLAFKVFGFKPPIPVPEQKDPDPDFSTVKCPNPEEGESVLELSLRLA 341
Cdd:PTZ00150 214 TLKSEyNPACCDRSK--VKIVYTAMHGVGTRFVQKALHTVGLPNLLSVAQQAEPDPEFPTVTFPNPEEGKGALKLSMETA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 342 EKENARVVLATDPDADRLAAAELQENGcWKVFTGNELAALFGWWMfdcWKKNKSRNADVKNVYMLATTVSSKILKAIALK 421
Cdd:PTZ00150 292 EAHGSTVVLANDPDADRLAVAEKLNNG-WKIFTGNELGALLAWWA---MKRYRRQGIDKSKCFFICTVVSSRMLKKMAEK 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 422 EGFHFEETLPGFKWIGSRIIDLL-ENGKEVLFAFEESIGFLCGTSVLDKDGVSAAVVVAEMASYLETMNITLKQQLVKVY 500
Cdd:PTZ00150 368 EGFQYDETLTGFKWIGNKAIELNaENGLTTLFAYEEAIGFMLGTRVRDKDGVTAAAVVAEMALYLYERGKTLVEHLESLY 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 501 EKYGYHISKTSYFLCYEPPTIKSIFERLRNFDSpkeYPKFCGTFAILHVRDVTTGYDSSQPNKKSVLPVSKNSQMITFTF 580
Cdd:PTZ00150 448 KQYGYHFTNNSYYICYDPSRIVSIFNDIRNNGS---YPTKLGGYPVTRIRDLTTGYDTATPDGKPLLPVSASTQMITFYF 524
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767967976 581 QNGCVATLRTSGTEPKIKYYAEMCASPDQSdtalLEEELKKLIDALIENFLQPSKNGLIWRS 642
Cdd:PTZ00150 525 ENGAIITIRGSGTEPKLKWYAELSGTKDEA----VEKELAALVDEVVEQLMQPEKYGLVPRK 582
|
|
| PGM2 |
cd05799 |
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The ... |
85-628 |
0e+00 |
|
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The mammalian PGM2 is thought to be a phosphopentomutase that catalyzes the conversion of the nucleoside breakdown products, ribose-1-phosphate and deoxyribose-1-phosphate to the corresponding 5-phosphopentoses. PGM2L1 is thought to catalyze the 1,3-bisphosphoglycerate-dependent synthesis of glucose 1,6-bisphosphate and other aldose-bisphosphates that serve as cofactors for several sugar phosphomutases and possibly also as regulators of glycolytic enzymes. PGM2 and PGM2L1 belong to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100092 Cd Length: 487 Bit Score: 680.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 85 RMTFGTAGLRSAMGAGFCYINDLTVIQSTQGMYKYLERCFSDFKQRGFVVGYDTRGqvtsscSSQRLAKLTAAVLLAKDV 164
Cdd:cd05799 1 RLEFGTAGLRGKMGAGTNRMNDYTVRQATQGLANYLKKKGPDAKNRGVVIGYDSRH------NSREFAELTAAVLAANGI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 165 PVYLFSRYVPTPFVPYAVQKLKAVAGVMITASHNRKEDNGYKVYWETGAQITSPHDKEILKCIEECVEPWNGSWNDNLvd 244
Cdd:cd05799 75 KVYLFDDLRPTPLLSFAVRHLGADAGIMITASHNPKEYNGYKVYWEDGAQIIPPHDAEIAEEIEAVLEPLDIKFEEAL-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 245 TSPLKRDPLQDICRRYMEDLKKICFYRELNSKTTLKFVHTSFHGVGHDYVQLAFKVFGFKPPIPVPEQKDPDPDFSTVKC 324
Cdd:cd05799 153 DSGLIKYIGEEIDDAYLEAVKKLLVNPELNEGKDLKIVYTPLHGVGGKFVPRALKEAGFTNVIVVEEQAEPDPDFPTVKF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 325 PNPEEgESVLELSLRLAEKENARVVLATDPDADRLAAAELQENGCWKVFTGNELAALFGWWMFDCWKKNKSrnaDVKNVY 404
Cdd:cd05799 233 PNPEE-PGALDLAIELAKKVGADLILATDPDADRLGVAVKDKDGEWRLLTGNEIGALLADYLLEQRKEKGK---LPKNPV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 405 MLATTVSSKILKAIALKEGFHFEETLPGFKWIGSRIIDLLENGKEVLFAFEESIGFLCGTSVLDKDGVSAAVVVAEMASY 484
Cdd:cd05799 309 IVKTIVSSELLRKIAKKYGVKVEETLTGFKWIGNKIEELESGGKKFLFGFEESIGYLVGPFVRDKDGISAAALLAEMAAY 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 485 LETMNITLKQQLVKVYEKYGYHISKTSYFLCYE---PPTIKSIFERLRNfdspkeypkfcgtfailhvrdvttgydssqp 561
Cdd:cd05799 389 LKAQGKTLLDRLDELYEKYGYYKEKTISITFEGkegPEKIKAIMDRLRN------------------------------- 437
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767967976 562 nkksvlpvskNSQMITFTFQNGCVATLRTSGTEPKIKYYAEMCASPDqsdtallEEELKKLIDALIE 628
Cdd:cd05799 438 ----------NPNVLTFYLEDGSRVTVRPSGTEPKIKFYIEVVGKKT-------LEEAEKKLDALKK 487
|
|
| ManB |
COG1109 |
Phosphomannomutase [Carbohydrate transport and metabolism]; |
85-627 |
1.26e-85 |
|
Phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440726 [Multi-domain] Cd Length: 456 Bit Score: 275.54 E-value: 1.26e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 85 RMTFGTAGLRSAMGAgfcYINDLTVIQSTQGMYKYLERCfsdfKQRGFVVGYDTRgqvtssCSSQRLAKLTAAVLLAKDV 164
Cdd:COG1109 4 KKLFGTDGIRGIVGE---ELTPEFVLKLGRAFGTYLKEK----GGPKVVVGRDTR------LSSPMLARALAAGLASAGI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 165 PVYLFsRYVPTPFVPYAVQKLKAVAGVMITASHNRKEDNGYKVYWETGAQITSPHDKEILKCIEEcVEPWNGSWNDNlvd 244
Cdd:COG1109 71 DVYDL-GLVPTPALAFAVRHLGADGGIMITASHNPPEYNGIKFFDADGGKLSPEEEKEIEALIEK-EDFRRAEAEEI--- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 245 tSPLKRdpLQDICRRYMEDLKKicFYRELNSKTTLKFVHTSFHGVGHDYVQLAFKVFGFKpPIPVPEQkdPDPDFSTVKc 324
Cdd:COG1109 146 -GKVTR--IEDVLEAYIEALKS--LVDEALRLRGLKVVVDCGNGAAGGVAPRLLRELGAE-VIVLNAE--PDGNFPNHN- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 325 PNPEEGesVLELSLRLAEKENARVVLATDPDADRLAAAElqENGcwKVFTGNELAALFGWWMfdcwkKNKSRNADVknvy 404
Cdd:COG1109 217 PNPEPE--NLEDLIEAVKETGADLGIAFDGDADRLGVVD--EKG--RFLDGDQLLALLARYL-----LEKGPGGTV---- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 405 mLATTVSSKILKAIALKEGFHFEETLPGFKWIGSRIidlLENGkeVLFAFEESIGFLCGTSVLDKDGVSAAVVVAEMASY 484
Cdd:COG1109 282 -VVTVMSSLALEDIAEKHGGEVVRTKVGFKYIKEKM---RETG--AVLGGEESGGIIFPDFVPTDDGILAALLLLELLAK 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 485 LETmniTLKQqlvkVYEKYGYHISKTSYFLCYEPPTIKSIFERLRNfdspkeypkfcgtfAILHVRDVTTgydssqpnkk 564
Cdd:COG1109 356 QGK---SLSE----LLAELPRYPQPEINVRVPDEEKIGAVMEKLRE--------------AVEDKEELDT---------- 404
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767967976 565 svlpvsknSQMITFTFQNGCVATLRTSGTEPKIKYYAEmcaSPDQSDTALLEEELKKLIDALI 627
Cdd:COG1109 405 --------IDGVKVDLEDGGWVLVRPSGTEPLLRVYAE---AKDEEEAEELLAELAELVEEAL 456
|
|
| phosphohexomutase |
cd03084 |
The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a ... |
188-623 |
8.26e-67 |
|
The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Members of this family include the phosphoglucomutases (PGM1 and PGM2), phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). These enzymes play important and diverse roles in carbohydrate metabolism in organisms from bacteria to humans. Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100086 [Multi-domain] Cd Length: 355 Bit Score: 222.62 E-value: 8.26e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 188 VAGVMITASHNRKEDNGYKVYWETGAQITSPHDKEILKCIEECVEPWNGSWNdnlvdtsPLKRDPLQDICRRYMEDLKKI 267
Cdd:cd03084 30 TGGIMITASHNPPEDNGIKFVDPDGEPIASEEEKAIEDLAEKEDEPSAVAYE-------LGGSVKAVDILQRYFEALKKL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 268 CFYRELNsKTTLKFVHTSFHGVGHDYVQLAFKVFGFKppiPVPEQKDPDPDFsTVKCPNPEEGESVLELSLRLaEKENAR 347
Cdd:cd03084 103 FDVAALS-NKKFKVVVDSVNGVGGPIAPQLLEKLGAE---VIPLNCEPDGNF-GNINPDPGSETNLKQLLAVV-KAEKAD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 348 VVLATDPDADRLAAAElqENgcWKVFTGNELAALFGWWMFDCWKKNKsrnadvknvYMLATTVSSKILKAIALKEGFHFE 427
Cdd:cd03084 177 FGVAFDGDADRLIVVD--EN--GGFLDGDELLALLAVELFLTFNPRG---------GVVKTVVSSGALDKVAKKLGIKVI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 428 ETLPGFKWIGSRIIDllengKEVLFAFEESIGFLCGTSVLDKDGVSAAVVVAEMASYLetmNITLKQQLVKVYEKYGYHI 507
Cdd:cd03084 244 RTKTGFKWVGEAMQE-----GDVVLGGEESGGVIFPEFHPGRDGISAALLLLEILANL---GKSLSELFSELPRYYYIRL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 508 SKTSYFLcyepptiksiferlrnfdspkeypkfcgtfailhvrdvttgydssqpnkksvlpvsknsqmitftfqngcvat 587
Cdd:cd03084 316 KVRGWVL------------------------------------------------------------------------- 322
|
410 420 430
....*....|....*....|....*....|....*.
gi 767967976 588 LRTSGTEPKIKYYAEMCAspdQSDTALLEEELKKLI 623
Cdd:cd03084 323 VRASGTEPAIRIYAEADT---QEDVEQIKKEARELV 355
|
|
| PGM_like2 |
cd05800 |
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
86-623 |
4.69e-61 |
|
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the alpha-D-phosphohexomutase superfamily and is found in both archaea and bacteria. The alpha-D-phosphohexomutases include several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four structural domains (subdomains) with a centrally located active site formed by four loops, one from each subdomain. All four subdomains are included in this alignment model.
Pssm-ID: 100093 Cd Length: 461 Bit Score: 210.49 E-value: 4.69e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 86 MTFGTAGLRSAMGAGFCYINDLTViqsTQGMYKYLERcfSDFKQRGFVVGYDTRGQvtsscsSQRLAKLTAAVLLAKDVP 165
Cdd:cd05800 1 IKFGTDGWRGIIAEDFTFENVRRV---AQAIADYLKE--EGGGGRGVVVGYDTRFL------SEEFARAVAEVLAANGID 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 166 VYLFSRYVPTPFVPYAVQKLKAVAGVMITASHNRKEDNGYKVYWETGAqitsPHDKEILKCIEECVEPWNGSWNDNLVDT 245
Cdd:cd05800 70 VYLSDRPVPTPAVSWAVKKLGAAGGVMITASHNPPEYNGVKVKPAFGG----SALPEITAAIEARLASGEPPGLEARAEG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 246 SPLKRDPLQDicrrYMEDLKKIcFYRELNSKTTLKFVHTSFHGVGHDYVQLAFKVFGFKppipVPE-QKDPDPDFStVKC 324
Cdd:cd05800 146 LIETIDPKPD----YLEALRSL-VDLEAIREAGLKVVVDPMYGAGAGYLEELLRGAGVD----VEEiRAERDPLFG-GIP 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 325 PNPEEgESVLELSLRLAEkENARVVLATDPDADRLAAAElqENGcwKVFTGNELAALFgwwMFDCWKKNKSRNADVKNVy 404
Cdd:cd05800 216 PEPIE-KNLGELAEAVKE-GGADLGLATDGDADRIGAVD--EKG--NFLDPNQILALL---LDYLLENKGLRGPVVKTV- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 405 mlATTVsskILKAIALKEGFHFEETLPGFKWIGSRIIDllengKEVLFAFEESIGFLCGTSVLDKDGVSAAVVVAEMASY 484
Cdd:cd05800 286 --STTH---LIDRIAEKHGLPVYETPVGFKYIAEKMLE-----EDVLIGGEESGGLGIRGHIPERDGILAGLLLLEAVAK 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 485 LETmniTLKQQLVKVYEKYGYHisktsYF----LCYEPPTIKSIFERLRNfdspkEYPKFCGTFAILHVRDVtTGYdssq 560
Cdd:cd05800 356 TGK---PLSELVAELEEEYGPS-----YYdridLRLTPAQKEAILEKLKN-----EPPLSIAGGKVDEVNTI-DGV---- 417
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767967976 561 pnKksvlpvsknsqmitFTFQNGCVATLRTSGTEPKIKYYAEMcasPDQSDTALLEEELKKLI 623
Cdd:cd05800 418 --K--------------LVLEDGSWLLIRPSGTEPLLRIYAEA---PSPEKVEALLDAGKKLA 461
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
85-229 |
1.54e-38 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
Pssm-ID: 427032 Cd Length: 138 Bit Score: 138.90 E-value: 1.54e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 85 RMTFGTAGLRSAMGAGFcyINDLTVIQSTQGMYKYLErcfSDFKQRGFVVGYDTRGqvtsscSSQRLAKLTAAVLLAKDV 164
Cdd:pfam02878 1 RQLFGTSGIRGKVGVGE--LTPEFALKLGQAIASYLR---AQGGGGKVVVGRDTRY------SSRELARALAAGLASNGV 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767967976 165 PVYLFSrYVPTPFVPYAVQKLKAVAGVMITASHNRKEDNGYKVYWETGAQITSPHDKEILKCIEE 229
Cdd:pfam02878 70 EVILLG-LLPTPAVSFATRKLKADGGIMITASHNPPEYNGIKVFDSNGGPIPPEVEKKIEAIIEK 133
|
|
| Arch_GlmM |
TIGR03990 |
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ... |
133-623 |
4.99e-27 |
|
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been characterized as the archaeal protein responsible for the second step of UDP-GlcNAc biosynthesis. This GlmM protein catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate. The first-characterized bacterial GlmM protein is modeled by TIGR01455. These two families are members of the larger phosphoglucomutase/phosphomannomutase family (characterized by three domains: pfam02878, pfam02879 and pfam02880), but are not nearest neighbors to each other. This model also includes a number of sequences from non-archaea in the Bacteroides, Chlorobi, Chloroflexi, Planctomycetes and Spirochaetes lineages. Evidence supporting their inclusion in this equivalog as having the same activity comes from genomic context and phylogenetic profiling. A large number of these organisms are known to produce exo-polysaccharide and yet only appeared to contain the GlmS enzyme of the GlmSMU pathway for UDP-GlcNAc biosynthesis (GenProp0750). In some organisms including Leptospira, this archaeal GlmM is found adjacent to the GlmS as well as a putative GlmU non-orthologous homolog. Phylogenetic profiling of the GlmS-only pattern using PPP identifies members of this archaeal GlmM family as the highest-scoring result. [Central intermediary metabolism, Amino sugars]
Pssm-ID: 274906 Cd Length: 443 Bit Score: 114.53 E-value: 4.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 133 VVGYDTRgqvtssCSSQRLAKLTAAVLLAKDVPVYLFSrYVPTPFVPYAVQKLKAVAGVMITASHNRKEDNGYKVYWETG 212
Cdd:TIGR03990 39 VVGRDTR------TSGPMLENAVIAGLLSTGCDVVDLG-IAPTPTLQYAVRELGADGGIMITASHNPPEYNGIKLLNSDG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 213 AQITSPHDKEILKCIEE---CVEPWNGswndnlvdTSPLKRDPlqDICRRYMED-LKKICfyRELNSKTTLKFVHTSFHG 288
Cdd:TIGR03990 112 TELSREQEEEIEEIAESgdfERADWDE--------IGTVTSDE--DAIDDYIEAiLDKVD--VEAIRKKGFKVVVDCGNG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 289 VGHDYVQLAFKVFGFKpPIPVPEQkdPDPDFSTvkcPNPEEGESVLELSLRLAEKENARVVLATDPDADRLAAaeLQENG 368
Cdd:TIGR03990 180 AGSLTTPYLLRELGCK-VITLNCQ--PDGTFPG---RNPEPTPENLKDLSALVKATGADLGIAHDGDADRLVF--IDEKG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 369 cwKVFTGNELAALFGWWMfdcWKKNKSRnadvknvymLATTVS-SKILKAIALKEGFHFEETLpgfkwIGSRII--DLLE 445
Cdd:TIGR03990 252 --RFIGGDYTLALFAKYL---LEHGGGK---------VVTNVSsSRAVEDVAERHGGEVIRTK-----VGEVNVaeKMKE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 446 NGkeVLFAFEESIGFLCGTSVLDKDGVSAAVVVAEMasyLETMNITLkQQLVKVYEKygYHISKTSyflcYEPPTIK--S 523
Cdd:TIGR03990 313 EG--AVFGGEGNGGWIFPDHHYCRDGLMAAALFLEL---LAEEGKPL-SELLAELPK--YPMSKEK----VELPDEDkeE 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 524 IFERLRnfdspKEYPKFcgtfailhvrDVTT--GydssqpnkksvlpvsknsqmITFTFQNGCVaTLRTSGTEPKIKYYA 601
Cdd:TIGR03990 381 VMEAVE-----EEFADA----------EIDTidG--------------------VRIDFEDGWV-LVRPSGTEPIVRIYA 424
|
490 500
....*....|....*....|..
gi 767967976 602 EmcaSPDQSDTALLEEELKKLI 623
Cdd:TIGR03990 425 E---AKTEERAEELLEEGRSLV 443
|
|
| PGM_like1 |
cd03087 |
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
125-623 |
2.42e-26 |
|
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. The alpha-D-phosphohexomutases include several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Members of this superfamily include the phosphoglucomutases (PGM1 and PGM2), phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100089 Cd Length: 439 Bit Score: 112.28 E-value: 2.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 125 SDFKQRGFVVGYDTRgqvtssCSSQRLAKLTAAVLLAKDVPVYLFSrYVPTPFVPYAVQKLkAVAGVMITASHNRKEDNG 204
Cdd:cd03087 29 TYLGGGTVVVGRDTR------TSGPMLKNAVIAGLLSAGCDVIDIG-IVPTPALQYAVRKL-GDAGVMITASHNPPEYNG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 205 YKVYWETGAQITSPHDKEILKCIEEcvEPWN-GSWNdnlvDTSPLKRDPlqDICRRYMED-LKKIcfyrELNSKTTLKFV 282
Cdd:cd03087 101 IKLVNPDGTEFSREQEEEIEEIIFS--ERFRrVAWD----EVGSVRRED--SAIDEYIEAiLDKV----DIDGGKGLKVV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 283 HTSFHGVGHDYVQLAFKVFGFKpPIPVPEQkdPDPDFSTvkcPNPEEGESVLELSLRLAEKENARVVLATDPDADRLAAa 362
Cdd:cd03087 169 VDCGNGAGSLTTPYLLRELGCK-VITLNAN--PDGFFPG---RPPEPTPENLSELMELVRATGADLGIAHDGDADRAVF- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 363 eLQENGcwKVFTGNELAALFGWWMfdCWKKNKSrnadvknvymLATTVS-SKILKAIALKEGFHFEETLpgfkwIGSRII 441
Cdd:cd03087 242 -VDEKG--RFIDGDKLLALLAKYL--LEEGGGK----------VVTPVDaSMLVEDVVEEAGGEVIRTP-----VGDVHV 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 442 DLLENGKEVLFAFEESIGFLCGTSVLDKDGVSAAVVVAEMASYLETMNitlkqQLVKVYEKygYHISKTSYflcyeppti 521
Cdd:cd03087 302 AEEMIENGAVFGGEPNGGWIFPDHQLCRDGIMTAALLLELLAEEKPLS-----ELLDELPK--YPLLREKV--------- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 522 ksiferlrnfDSPKEYPKfcgtfAIL-HVRDVTTGYDssqpnkKSVLPVSKnsqmITFTFQNGCVaTLRTSGTEPKIKYY 600
Cdd:cd03087 366 ----------ECPDEKKE-----EVMeAVEEELSDAD------EDVDTIDG----VRIEYEDGWV-LIRPSGTEPKIRIT 419
|
490 500
....*....|....*....|...
gi 767967976 601 AEmcaSPDQSDTALLEEELKKLI 623
Cdd:cd03087 420 AE---AKTEERAKELLEEGRSKV 439
|
|
| PGM_PMM_II |
pfam02879 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II; |
260-368 |
4.74e-23 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II;
Pssm-ID: 427033 Cd Length: 102 Bit Score: 93.89 E-value: 4.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 260 YMEDLKKICFyRELNSKTTLKFVHTSFHGVGHDYVQLAFKVFGFkppIPVPEQKDPDPDFSTvKCPNPEEGEsVLELSLR 339
Cdd:pfam02879 2 YIDHLLELVD-SEALKKRGLKVVYDPLHGVGGGYLPELLKRLGC---DVVEENCEPDPDFPT-RAPNPEEPE-ALALLIE 75
|
90 100
....*....|....*....|....*....
gi 767967976 340 LAEKENARVVLATDPDADRLAAAElqENG 368
Cdd:pfam02879 76 LVKSVGADLGIATDGDADRLGVVD--ERG 102
|
|
| PMM_PGM |
cd03089 |
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the ... |
133-382 |
4.11e-18 |
|
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the reversible conversion of 1-phospho to 6-phospho-sugars (e.g. between mannose-1-phosphate and mannose-6-phosphate or glucose-1-phosphate and glucose-6-phosphate) via a bisphosphorylated sugar intermediate. The reaction involves two phosphoryl transfers, with an intervening 180 degree reorientation of the reaction intermediate during catalysis. Reorientation of the intermediate occurs without dissociation from the active site of the enzyme and is thus, a simple example of processivity, as defined by multiple rounds of catalysis without release of substrate. Glucose-6-phosphate and glucose-1-phosphate are known to be utilized for energy metabolism and cell surface construction, respectively. PMM/PGM belongs to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the phosphoglucomutases (PGM1 and PGM2). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100091 Cd Length: 443 Bit Score: 87.18 E-value: 4.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 133 VVGYDTRgqvtssCSSQRLAKLTAAVLLAKDVPVYLFSRyVPTPFVPYAVQKLKAVAGVMITASHNRKEDNGYKvyWETG 212
Cdd:cd03089 40 VVGRDGR------LSSPELAAALIEGLLAAGCDVIDIGL-VPTPVLYFATFHLDADGGVMITASHNPPEYNGFK--IVIG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 213 AQITSPHD-KEILKCIEecvepwNGSWNDNLVDTSPLKRDPLQDICRRYMEDLKKicfyrelnSKTTLKFVHTSFHGVGH 291
Cdd:cd03089 111 GGPLSGEDiQALRERAE------KGDFAAATGRGSVEKVDILPDYIDRLLSDIKL--------GKRPLKVVVDAGNGAAG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 292 DYVQLAFKVFGFKppiPVPEQKDPDPDFSTvKCPNPEEGESVLELSLRLAEkENARVVLATDPDADRLAAaeLQENGcwK 371
Cdd:cd03089 177 PIAPQLLEALGCE---VIPLFCEPDGTFPN-HHPDPTDPENLEDLIAAVKE-NGADLGIAFDGDGDRLGV--VDEKG--E 247
|
250
....*....|.
gi 767967976 372 VFTGNELAALF 382
Cdd:cd03089 248 IIWGDRLLALF 258
|
|
| PGM_PMM_III |
pfam02880 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III; |
374-503 |
2.34e-15 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III;
Pssm-ID: 460733 Cd Length: 115 Bit Score: 72.48 E-value: 2.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 374 TGNELAALFGWWMFDcwKKNKSRNADVknvymLATTVSSKILKAIALKEGFHFEETLPGFKWIGSRiidLLENGkeVLFA 453
Cdd:pfam02880 1 DGDQILALLAKYLLE--QGKLPPGAGV-----VKTVMSSLGLDRVAKKLGGKLVRTPVGDKYVKEK---MREEG--ALFG 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 767967976 454 FEESIGFLCGTSVLDKDGVSAAVVVAEMASYletMNITLKQQLVKVYEKY 503
Cdd:pfam02880 69 GEESGHIIFLDHATTKDGILAALLVLEILAR---TGKSLSELLEELPEKY 115
|
|
| PGM_like4 |
cd05803 |
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate ... |
123-360 |
3.21e-14 |
|
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate guanyltransferase domain in a protein of unknown function that is found in both prokaryotes and eukaryotes. This domain belongs to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Members of this superfamily include the phosphoglucomutases (PGM1 and PGM2), phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100096 Cd Length: 445 Bit Score: 75.42 E-value: 3.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 123 CFSDFKQRGFVVGYDTRGqvtsscSSQRLAKLTAAVLLA--KDVpVYLfsRYVPTPFVPYAVQKLKAVAGVMITASHNRK 200
Cdd:cd05803 31 QPERTKGGKIVVGRDGRP------SGPMLEKIVIGALLAcgCDV-IDL--GIAPTPTVQVLVRQSQASGGIIITASHNPP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 201 EDNGYKVYWETGAQITSPHDKEILKCIEECVEPWNGswNDNL--VDTSPlkrDPLQDicrrYMED-LKKICFYRELNSKT 277
Cdd:cd05803 102 QWNGLKFIGPDGEFLTPDEGEEVLSCAEAGSAQKAG--YDQLgeVTFSE---DAIAE----HIDKvLALVDVDVIKIRER 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 278 TLKFVHTSFHGVGHDYV-----QL--AFKVFGFKPPIPVPEQKDPDPdfstvkcpnpeegESVLELSlRLAEKENARVVL 350
Cdd:cd05803 173 NFKVAVDSVNGAGGLLIprlleKLgcEVIVLNCEPTGLFPHTPEPLP-------------ENLTQLC-AAVKESGADVGF 238
|
250
....*....|
gi 767967976 351 ATDPDADRLA 360
Cdd:cd05803 239 AVDPDADRLA 248
|
|
| PGM_like3 |
cd05801 |
This bacterial PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
85-628 |
1.93e-11 |
|
This bacterial PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the alpha-D-phosphohexomutase superfamily. The alpha-D-phosphohexomutases include several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100094 [Multi-domain] Cd Length: 522 Bit Score: 66.89 E-value: 1.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 85 RMTFGTAGLR-SAMGAGFcyiNDLTVIQSTQGMYKYleRcfsdfKQRGF----VVGYDTRGQvtsscssQRLAKLTA-AV 158
Cdd:cd05801 20 RVAFGTSGHRgSSLKGSF---NEAHILAISQAICDY--R-----KSQGItgplFLGKDTHAL-------SEPAFISAlEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 159 LLAKDVPVYLFSR--YVPTPFVPYAV-----QKLKAVA-GVMITASHNRKEDNGYKVYWETGAqitsPHDKEILKCIEEC 230
Cdd:cd05801 83 LAANGVEVIIQQNdgYTPTPVISHAIltynrGRTEGLAdGIVITPSHNPPEDGGFKYNPPHGG----PADTDITRWIEKR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 231 VepwNGSWNDNLVDtspLKRDPL-----------QDICRRYMEDLKKIcfyreLN----SKTTLKFVHTSFHGVGHDYVQ 295
Cdd:cd05801 159 A---NALLANGLKG---VKRIPLeaalasgythrHDFVTPYVADLGNV-----IDmdaiRKSGLRLGVDPLGGASVPYWQ 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 296 LAFKVFGFKPPIPVPEQkDPDPDFSTV--------KCPNPEEGESVLELslrlaeKENARVVLATDPDADRLAAAElqen 367
Cdd:cd05801 228 PIAEKYGLNLTVVNPKV-DPTFRFMTLdhdgkirmDCSSPYAMAGLLKL------KDKFDLAFANDPDADRHGIVT---- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 368 GCWKVFTGNELAALFGWWMFdcwkknKSRNADVKNVYMLATTVSSKILKAIALKEGFHFEETLPGFKWigsrIIDLLENG 447
Cdd:cd05801 297 PSAGLMNPNHYLSVAIDYLF------THRPLWNKSAGVGKTLVSSSMIDRVAAALGRKLYEVPVGFKW----FVDGLLDG 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 448 KeVLFAFEESIG--FLC--GTS-VLDKDGVSAAVVVAEMasyLETMNITLKQQLVKVYEKYGYHIsktsYFLCYEP--PT 520
Cdd:cd05801 367 S-LGFGGEESAGasFLRrdGTVwTTDKDGIIMCLLAAEI---LAVTGKDPGQLYQELTERFGEPY----YARIDAPatPE 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 521 IKSIFERLrnfdSPKE-YPKFCGTFAILHVRDVTTGYDSSQPNKKsvlpvsknsqmitFTFQNGCVAtLRTSGTEPKIKY 599
Cdd:cd05801 439 QKARLKKL----SPEQvTATELAGDPILAKLTRAPGNGASIGGLK-------------VTTANGWFA-ARPSGTEDVYKI 500
|
570 580
....*....|....*....|....*....
gi 767967976 600 YAEMCASpdqsdtallEEELKKLIDALIE 628
Cdd:cd05801 501 YAESFLS---------EEHLKKIQKEAQE 520
|
|
| GlmM |
cd05802 |
GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the ... |
132-232 |
8.11e-11 |
|
GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the alpha-D-phosphohexomutase superfamily. It is required for the interconversion of glucosamine-6-phosphate and glucosamine-1-phosphate in the biosynthetic pathway of UDP-N-acetylglucosamine, an essential precursor to components of the cell envelope. In order to be active, GlmM must be phosphorylated, which can occur via autophosphorylation or by the Ser/Thr kinase StkP. GlmM functions in a classical ping-pong bi-bi mechanism with glucosamine-1,6-diphosphate as an intermediate. Other members of the alpha-D-phosphohexomutase superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100095 Cd Length: 434 Bit Score: 64.43 E-value: 8.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 132 FVVGYDTRgqvtssCSSQRLAKLTAAVLLAKDVPVYLFSrYVPTPFVPYAVQKLKAVAGVMITASHNRKEDNGYKVYWET 211
Cdd:cd05802 40 VLIGKDTR------ISGYMLESALAAGLTSAGVDVLLLG-VIPTPAVAYLTRKLRADAGVVISASHNPFEDNGIKFFSSD 112
|
90 100
....*....|....*....|.
gi 767967976 212 GAQItsPHDKEILkcIEECVE 232
Cdd:cd05802 113 GYKL--PDEVEEE--IEALID 129
|
|
| glmM |
TIGR01455 |
phosphoglucosamine mutase; This model describes GlmM, phosphoglucosamine mutase, also ... |
133-208 |
7.16e-10 |
|
phosphoglucosamine mutase; This model describes GlmM, phosphoglucosamine mutase, also designated in MrsA and YhbF E. coli, UreC in Helicobacter pylori, and femR315 or FemD in Staphlococcus aureus. It converts glucosamine-6-phosphate to glucosamine-1-phosphate as part of the pathway toward UDP-N-acetylglucosamine for peptidoglycan and lipopolysaccharides. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Central intermediary metabolism, Amino sugars]
Pssm-ID: 130522 Cd Length: 443 Bit Score: 61.61 E-value: 7.16e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767967976 133 VVGYDTRgqvtssCSSQRLAKLTAAVLLAKDVPVYLFSrYVPTPFVPYAVQKLKAVAGVMITASHNRKEDNGYKVY 208
Cdd:TIGR01455 42 VIGKDTR------LSGYMLENALAAGLNSAGVDVLLLG-PLPTPAVAYLTRTLRADAGVMISASHNPYEDNGIKFF 110
|
|
| ManB |
cd03088 |
ManB is a bacterial phosphomannomutase (PMM) that catalyzes the conversion of mannose ... |
88-225 |
1.52e-06 |
|
ManB is a bacterial phosphomannomutase (PMM) that catalyzes the conversion of mannose 6-phosphate to mannose-1-phosphate in the second of three steps in the GDP-mannose pathway, in which GDP-D-mannose is synthesized from fructose-6-phosphate. In Mycobacterium tuberculosis, the causative agent of tuberculosis, PMM is involved in the biosynthesis of mannosylated lipoglycans that participate in the association of mycobacteria with host macrophage phagocytic receptors. ManB belongs to the the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include the phosphoglucomutases (PGM1 and PGM2), phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100090 Cd Length: 459 Bit Score: 51.05 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767967976 88 FGTAGLR---SAMGAGFCYINdltviqsTQGMYKYLErcfSDFKQRGFVVGYDTRGqvtsscSSQRLAKLTAAVLLAKDV 164
Cdd:cd03088 2 FGTSGLRglvTDLTDEVCYAY-------TRAFLQHLE---SKFPGDTVAVGRDLRP------SSPRIAAACAAALRDAGF 65
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767967976 165 -PVYLFSryVPTPFVPYAVQKLKAvAGVMITASHNRKEDNGYKVYWETGaqitsphdkEILK 225
Cdd:cd03088 66 rVVDCGA--VPTPALALYAMKRGA-PAIMVTGSHIPADRNGLKFYRPDG---------EITK 115
|
|
| glmM |
PRK10887 |
phosphoglucosamine mutase; Provisional |
173-206 |
3.08e-05 |
|
phosphoglucosamine mutase; Provisional
Pssm-ID: 236787 Cd Length: 443 Bit Score: 46.67 E-value: 3.08e-05
10 20 30
....*....|....*....|....*....|....
gi 767967976 173 VPTPFVPYAVQKLKAVAGVMITASHNRKEDNGYK 206
Cdd:PRK10887 76 MPTPAVAYLTRTLRAEAGIVISASHNPYYDNGIK 109
|
|
| PGM3 |
cd03086 |
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 ... |
186-207 |
5.66e-04 |
|
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 (N-acetylglucosamine-phosphate mutase), is an essential enzyme found in eukaryotes that reversibly catalyzes the conversion of GlcNAc-6-phosphate into GlcNAc-1-phosphate as part of the UDP-N-acetylglucosamine (UDP-GlcNAc) biosynthetic pathway. UDP-GlcNAc is an essential metabolite that serves as the biosynthetic precursor of many glycoproteins and mucopolysaccharides. AGM1 is a member of the alpha-D-phosphohexomutase superfamily, which catalyzes the intramolecular phosphoryl transfer of sugar substrates. The alpha-D-phosphohexomutases have four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100088 Cd Length: 513 Bit Score: 42.97 E-value: 5.66e-04
|
| PLN02895 |
PLN02895 |
phosphoacetylglucosamine mutase |
184-207 |
9.46e-04 |
|
phosphoacetylglucosamine mutase
Pssm-ID: 215485 Cd Length: 562 Bit Score: 42.32 E-value: 9.46e-04
10 20
....*....|....*....|....
gi 767967976 184 KLKAVAGVMITASHNRKEDNGYKV 207
Cdd:PLN02895 55 KTGAATGLMITASHNPVSDNGVKI 78
|
|
| PTZ00302 |
PTZ00302 |
N-acetylglucosamine-phosphate mutase; Provisional |
576-629 |
1.04e-03 |
|
N-acetylglucosamine-phosphate mutase; Provisional
Pssm-ID: 240352 [Multi-domain] Cd Length: 585 Bit Score: 41.95 E-value: 1.04e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 767967976 576 ITFTFQNGCVATLRTSGTEPKIKYYAEmcaSPDQSDTALLEEELKKLIDALIEN 629
Cdd:PTZ00302 534 IVSKYDNAARAFIRPSGTEPVVRVYAE---APTLEQADELANEVKGLVLRYCSG 584
|
|
| PGM_PMM_IV |
pfam00408 |
Phosphoglucomutase/phosphomannomutase, C-terminal domain; |
573-623 |
1.07e-03 |
|
Phosphoglucomutase/phosphomannomutase, C-terminal domain;
Pssm-ID: 425666 Cd Length: 71 Bit Score: 38.02 E-value: 1.07e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 767967976 573 SQMITFTFQNGCVATLRTSGTEPKIKYYAEmcaSPDQSDTALLEEELKKLI 623
Cdd:pfam00408 23 ADAEKILGEDGRRLDVRPSGTEPVLRVMVE---GDSDEELARLADEIADLL 70
|
|
| |
